Isolation and Amino Acid Sequences of Tropoelastin Peptides

• Published in: The Journal of biological chemistry Vol. 248; no. 8; pp. 2876 - 2879
• Main Authors: Foster, J A, Bruenger, E, Gray, W R, Sandberg, L B
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 25-04-1973
• Subjects: Amino Acid Sequence; Animals; Aorta; Chromatography, Gas; Copper; Deficiency Diseases - metabolism; Elastin - analysis; Peptides - isolation & purification; Solubility; Swine; Trypsin
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(19)44088-x

Seventeen peptides have been isolated from a tryptic digest of soluble elastin by ion exchange chromatography and gel filtration.
Molecular weights range from approximately 1,700 to 10,500. Partial or complete amino acid sequences of the peptides were
obtained and provide the first extensive data on the primary sequence of elastin. Several important findings stand out. First,
the sequences obtained reveal an elastin primary structure quite distinct from collagen and possessing repeats of a tetrapeptide,
Gly-Gly-Val-Pro, a pentapeptide, Pro-Gly-Val-Gly-Val, and a hexapeptide, Pro-Gly-Val-Gly-Val-Ala. Second, several of the peptides
contain a partial hydroxylation of proline residues thereby definitely establishing hydroxyproline as a real constituent of
the elastin chain.